Relevant bibliographies by topics / Cytochrome C oxidase

Academic literature on the topic 'Cytochrome C oxidase'

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Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "Cytochrome C oxidase"

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Otten, Marijke F., John van der Oost, Willem N. M. Reijnders, Hans V. Westerhoff, Bernd Ludwig, and Rob J. M. Van Spanning. "Cytochromes c550,c552, and c1 in the Electron Transport Network of Paracoccus denitrificans: Redundant or Subtly Different in Function?" Journal of Bacteriology 183, no. 24 (December 15, 2001): 7017–26. http://dx.doi.org/10.1128/jb.183.24.7017-7026.2001.

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ABSTRACT Paracoccus denitrificans strains with mutations in the genes encoding the cytochrome c 550,c 552, or c 1 and in combinations of these genes were constructed, and their growth characteristics were determined. Each mutant was able to grow heterotrophically with succinate as the carbon and free-energy source, although their specific growth rates and maximum cell numbers fell variably behind those of the wild type. Maximum cell numbers and rates of growth were also reduced when these strains were grown with methylamine as the sole free-energy source, with the triple cytochromec mutant failing to grow on this substrate. Under anaerobic conditions in the presence of nitrate, none of the mutant strains lacking the cytochrome bc 1 complex reduced nitrite, which is cytotoxic and accumulated in the medium. The cytochrome c 550-deficient mutant did denitrify provided copper was present. The cytochromec 552 mutation had no apparent effect on the denitrifying potential of the mutant cells. The studies show that the cytochromes c have multiple tasks in electron transfer. The cytochrome bc 1 complex is the electron acceptor of the Q-pool and of amicyanin. It is also the electron donor to cytochromes c 550 andc 552 and to thecbb 3-type oxidase. Cytochromec 552 is an electron acceptor both of the cytochrome bc 1 complex and of amicyanin, as well as a dedicated electron donor to theaa 3-type oxidase. Cytochromec 550 can accept electrons from the cytochrome bc 1 complex and from amicyanin, whereas it is also the electron donor to both cytochromec oxidases and to at least the nitrite reductase during denitrification. Deletion of the c-type cytochromes also affected the concentrations of remaining cytochromes c, suggesting that the organism is plastic in that it adjusts its infrastructure in response to signals derived from changed electron transfer routes.
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Kornblatt, Jack A., Janice Theodorakis, Gaston Hui Bon Hoa, and Emmanuel Margoliash. "Cytochrome c and cytochrome c oxidase interactions: the effects of ionic strength and hydrostatic pressure studied with site-specific modifications of cytochrome c." Biochemistry and Cell Biology 70, no. 7 (July 1, 1992): 539–47. http://dx.doi.org/10.1139/o92-084.

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Seven cytochromes c, in which individual lysines have been modified to the propylthiobimane derivatives, have been prepared. These derivatives were also converted to the porphyrin cytochromes c by treatment with HF. The properties of both types of modified proteins were studied in their reactions with cytochrome c oxidase. The results show that lysines 25, 27, 60, 72, and 87 do not contribute a full charge to the binding interaction with the oxidase. These five residues, with the exception of the lysine-60 derivative, are on the front surface of the protein and contain the solvent-accessible edge of the heme prosthetic group. By contrast, lysines 8 and 13 at the top of the front surface do contribute a full charge to the binding interaction with the oxidase. The removal of the positive charge on any one lysine weakens the binding to cytochrome c oxidase by at least 1 kcal (1 cal = 4.1868 J). The presence of bimane at lysines 13 and 87 clearly forces the separation of the cytochrome c and oxidase, but this does not occur with the other complexes. The bimane-modified lysine-13 protein, and to a lesser extent that modified at lysine 8, show the interesting effect of enhanced complex formation with cytochrome c oxidase when subjected to pressure, possibly because of entrapment of water at the newly created interface of the complex. Our observations indicate that the two proteins of the cytochrome c – cytochrome oxidase complex have preferred, but not obligatory, spatial orientations and that interaction occurs without either protein losing significant portions of its hydration shell.Key words: cytochrome oxidase, cytochrome c, binding, hydrostatic pressure.
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Kossekova, G., B. Atanasov, R. Bolli, and A. Azzi. "Ionic-strength-dependence of the oxidation of native and pyridoxal 5′-phosphate-modified cytochromes c by cytochrome c oxidase." Biochemical Journal 262, no. 2 (September 1, 1989): 591–96. http://dx.doi.org/10.1042/bj2620591.

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The ionic-strength-dependences of the rate constants (log k plotted versus square root of 1) for oxidation of native and pyridoxal 5′-phosphate-modified cytochromes c by three different preparations of cytochrome c oxidase have complex non-linear character, which may be explained on the basis of present knowledge of the structure of the oxidase and the monomer-dimer equilibrium of the enzyme. The wave-type curve (with a minimum and a maximum) for oxidation of native cytochrome c by purified cytochrome c oxidase depleted of phospholipids may reflect consecutively inhibition of oxidase monomers (initial descending part), competition between this inhibition and dimer formation, resulting in increased activity (second part with positive slope), and finally inhibition of oxidase dimers (last descending part of the curve). The dependence of oxidation of native cytochrome c by cytochrome c oxidase reconstituted into phospholipid vesicles is a curve with a maximum, without the initial descending part described above. This may reflect the lack of pure monomers in the vesicles, where equilibrium is shifted to dimers even at low ionic strength. Subunit-III-depleted cytochrome c oxidase does not exhibit the maximum seen with the other two enzyme preparations. This may mean that removal of subunit III hinders dimer formation. The charge interactions of each of the cytochromes c (native or modified) with the three cytochrome c oxidase preparations are similar, as judged by the similar slopes of the linear dependences at I values above the optimal one. This shows that subunit III and the phospholipid membrane do not seem to be involved in the specific charge interaction of cytochrome c oxidase with cytochrome c.
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Sampson, Valerie, and Trevor Alleyne. "Cytochrome c /cytochrome c oxidase interaction." European Journal of Biochemistry 268, no. 24 (December 15, 2001): 6534–44. http://dx.doi.org/10.1046/j.0014-2956.2001.02608.x.

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Ostermeier, C. "Cytochrome c oxidase." Current Opinion in Structural Biology 6, no. 4 (August 1996): 460–66. http://dx.doi.org/10.1016/s0959-440x(96)80110-2.

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Taanman, J. W., and S. L. Williams. "Assembly of cytochrome c oxidase: what can we learn from patients with cytochrome c oxidase deficiency?" Biochemical Society Transactions 29, no. 4 (August 1, 2001): 446–51. http://dx.doi.org/10.1042/bst0290446.

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Cytochrome c oxidase is an intricate metalloprotein that transfers electrons from cytochrome c to oxygen in the last step of the mitochondrial respiratory chain. It uses the free energy of this reaction to sustain a transmembrane electrochemical gradient of protons. Site-directed mutagenesis studies of bacterial terminal oxidases and the recent availability of refined crystal structures of the enzyme are rapidly expanding the understanding of the coupling mechanism between electron transfer and proton translocation. In contrast, relatively little is known about the assembly pathway of cytochrome c oxidase. Studies in yeast have indicated that assembly is dependent on numerous proteins in addition to the structural subunits and prosthetic groups. Human homologues of a number of these assembly factors have been identified and some are now known to be involved in disease. To dissect the assembly pathway of cytochrome c oxidase, we are characterizing tissues and cell cultures derived from patients with genetically defined cytochrome c oxidase deficiency, using biochemical, biophysical and immunological techniques. These studies have allowed us to identify some of the steps of the assembly process.
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Nicholls, Peter. "Control of proteoliposomal cytochrome c oxidase: the partial reactions." Biochemistry and Cell Biology 68, no. 9 (September 1, 1990): 1135–41. http://dx.doi.org/10.1139/o90-169.

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The steady-state spectroscopic behaviour and the turnover of cytochrome c oxidase incorporated into proteoliposomes have been investigated as functions of membrane potential and pH gradient. The respiration rate is almost linearly dependent on [cytochrome c2+] at high flux, but while the cytochrome a redox state is always dependent on the [cytochrome c2+] steady state, it reaches a maximum reduction level less than 100% in each case. The maximal aerobic steady-state reduction level of cytochrome a is highest in the presence of valinomycin and lowest in the presence of nigericin. The proportion of [cytochrome c2+] required to achieve 50% of maximal reduction of cytochrome a varies with the added ionophores; the apparent redox potential of cytochrome a is most positive in the fully decontrolled system (plus valinomycin and nigericin). At low levels of cytochrome a reduction, the rate of respiration is no longer a linear function of [cytochrome c2+], but is dependent upon the redox state of both cytochromes a and c. That is, proteoliposomal oxidase does not follow Smith–Conrad kinetics at low cytochrome c reduction levels, especially in the controlled states. The control of cytochrome oxidase turnover by ΔpH and by ΔΨ can be explained either by an allosteric model or by a model with reversed electron transfer between the binuclear centre and cytochrome a. Other evidence suggests that the reversed electron transfer model may be the correct one.Key words: proteoliposomes, cytochrome c, cytochrome oxidase, membrane potential, pH gradient, cytochrome a, electron transfer.
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Bengtsson, Jenny, Claes von Wachenfeldt, Lena Winstedt, Per Nygaard, and Lars Hederstedt. "CtaG is required for formation of active cytochrome c oxidase in Bacillus subtilis." Microbiology 150, no. 2 (February 1, 2004): 415–25. http://dx.doi.org/10.1099/mic.0.26691-0.

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The Gram-positive bacterium Bacillus subtilis contains two respiratory oxidases of the haem-copper superfamily: cytochrome aa 3, which is a quinol oxidase, and cytochrome caa 3, which is a cytochrome c oxidase. Cytochrome c oxidase uniquely contains a di-copper centre, CuA. B. subtilis CtaG is a membrane protein encoded by the same gene cluster as that which encodes the subunits of cytochrome c oxidase. The role of B. subtilis CtaG and orthologous proteins present in many other Gram-positive bacteria has remained unexplored. The sequence of CtaG is unrelated to that of CtaG/Cox11p of proteobacteria and eukaryotic cells. This study shows that B. subtilis CtaG is essential for the formation of active cytochrome caa 3 but is not required for assembly of the core subunits I and II with haem in the membrane and it has no role in the synthesis of active cytochrome aa 3. B. subtilis YpmQ, a homologue to Sco1p of eukaryotic cells, is also a membrane-bound cytochrome c oxidase-specific assembly factor. Properties of CtaG- and YpmQ-deficient mutants were compared. Cells lacking YpmQ showed a low cytochrome c oxidase activity and this defect was suppressed by the supplementation of the growth medium with copper ions. It has previously been proposed that YpmQ/Sco1p is involved in synthesis of the CuA centre. The results of this study are consistent with this proposal but the exact role of YpmQ in assembly of cytochrome c oxidase remains to be elucidated.
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Kopylchuk, H. P., and O. M. Voloshchuk. "Activity of respiratory chain cytochrome complexes and cytochromes content in the rat kidney mitochondria under different nutrients content in a diet." Ukrainian Biochemical Journal 95, no. 1 (April 26, 2023): 64–72. http://dx.doi.org/10.15407/ubj95.01.064.

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An important role in ensuring the functioning of the respiratory chain belongs to the cytochrome part, which includes complexes III (ubiquinol-cytochrome c oxidoreductase) and IV (cytochrome c oxidase). The key components of these enzymatic complexes are heme-containing cytochromes, the number of which depends on the balance of heme synthesis and catabolism. δ-Aminolevulinate synthase catalyzes the first step of the heme biosynthetic pathway, while heme oxygenase is the key enzyme of heme degradation. It is known that nutritional imbalances drive many risk factors for chronic kidney disease. That is why our research aimed to study the activity of ubiquinol-cytochrome c oxidoreductase and cytochrome oxidase complexes, the level of cytochromes a+a3, b, c, and c1, and the activity of key enzymes of heme metabolism in the mitochondria of rat kidneys under conditions of different content of protein and sucrose in animal diet. The obtained results showed a decreased activity of ubiquinol-cytochrome c oxidoreductase and cytochrome oxidase complexes and reduced levels of mitochondria cytochromes a+a3, b, c, and c1 in the kidney mitochondria under the conditions of nutrient imbalance, with the most pronounced changes found in animals kept on a low-protein/high-sucrose diet. A decrease in δ-aminolevulinate synthase activity with a simultaneous 2-fold increase in heme oxygenase activity was found in kidney mitochondria of animals kept on a low-protein/high-sucrose diet compared to those kept on full-value diet indicating an intensification of heme catabolism along with inhibition of its synthesis. The obtained results testify the energy imbalance under the conditions of low-protein/high-sucrose which in turn can lead to the progression of kidney injury. Keywords: cytochrome oxidase, cytochromes, heme oxygenase, nutrients, ubiquinol-cytochrome c oxidoreductase, δ-aminolevulinate synthase
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Shimokata, K., Y. Katayama, H. Shimada, and S. Yoshikawa. "hybrid cytochrome c oxidase." Seibutsu Butsuri 41, supplement (2001): S115. http://dx.doi.org/10.2142/biophys.41.s115_4.

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Dissertations / Theses on the topic "Cytochrome C oxidase"

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Howell, T. W. "Reconstituted cytochrome c oxidase vesicles." Thesis, University of Bristol, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.370702.

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Cappuccio, Jenny A. "Spectroscopic studies of cytochrome c oxidase /." Diss., Digital Dissertations Database. Restricted to UC campuses, 2004. http://uclibs.org/PID/11984.

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Lin, Jian Chan Sunney I. "ATP modulation of the electron transfer between cytochrome c and cytochrome c oxidase." Diss., Pasadena, Calif. : California Institute of Technology, 1995. http://resolver.caltech.edu/CaltechETD:etd-10182007-085924.

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Brändén, Gisela. "Structure and function of cytochrome c oxidase /." Stockholm : Department of Biochemistry and Biophysics, Stockholm University, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1226.

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Poynter, D. "Structural studies on bovine heart cytochrome c oxidase." Thesis, University of Nottingham, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.356539.

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Chrzanowska-Lightowlers, Zofia Maria Alexandra. "Regulation of the homeostasis of cytochrome C oxidase." Thesis, University of Newcastle Upon Tyne, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.260970.

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Adams, Paula Louise. "Cytochrome c oxidase deficiency : biochemical & molecular studies." Thesis, University of Newcastle Upon Tyne, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337193.

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Näsvik, Öjemyr Linda. "Membrane effects on proton transfer in cytochrome c oxidase." Doctoral thesis, Stockholms universitet, Institutionen för biokemi och biofysik, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-75633.

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The biological membrane is composed of lipids and proteins that make up dynamic barriers around cells and organelles. Membrane-spanning proteins are involved in many key processes in the cell such as energy conversion, nerve conduction and signal transduction. These proteins interact closely with lipids as well as with other proteins in the membrane, which modulates and affects their structure and function. In the energy-conversion process, membrane-bound proton-transport proteins maintain an electrochemical proton gradient across the mitochondrial inner membrane or the cytoplasmic membrane of bacteria. This gradient is utilized for ATP synthesis or transport of ions and molecules across the membrane. Results from earlier studies have shown that proton transporters are influenced by their environment. Here, one of these proton transporters, cytochrome c oxidase, has been purified and reconstituted into liposomes or nanodiscs and membrane effects on specific proton-transfer processes were studied. In these studies we observed that the membrane accelerated proton transfer to the surface of cytochrome c oxidase and that there is a protonic link, via a Glu residue that mediates proton transfer from the membrane surface to a proton-transfer pathway in this protein. In addition, the membrane was shown to modulate specific internal electron and proton-transfer reactions. The results from these studies show that the membrane composition influences transmembrane transport. Consequently, our understanding of these processes requires investigation of these transporter proteins in different membrane-mimetic systems of variable and well-defined composition. Furthermore, the data show that membrane surfaces facilitate lateral proton transfer which is presumably essential for maintaining high efficiency in energy conversion. This is particular important in organisms such as alkaliphilic bacteria where the driving force of the electrochemical proton gradient, between the bulk solution on each side of the membrane is not sufficient for ATP synthesis.
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Salomonsson, Lina. "Proton, Electron, and O₂ transfer in Cytochrome c Oxidase /." Stockholm : Department of Biochemistry and Biophysics, Stockholm university, 2006. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1222.

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El-Agez, Bassam Ali. "A kinetic and spectroscopic study on cytochrome c oxidase." Thesis, University of Essex, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.305116.

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Books on the topic "Cytochrome C oxidase"

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1955-, Gonzalez-Lima Francisco, ed. Cytochrome oxidase in neuronal metabolism and Alzheimer's disease. New York: Plenum Press, 1998.

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Functional and spectroscopic analysis of the cytochrome c: Cytochrome c oxidase interaction. 1993.

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Gonzalez-Lima, Francisco. Cytochrome Oxidase in Neuronal Metabolism and Alzheimer's Disease. Springer London, Limited, 2013.

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Book chapters on the topic "Cytochrome C oxidase"

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Schomburg, D., M. Salzmann, and D. Stephan. "Cytochrome-c oxidase." In Enzyme Handbook 7, 619–34. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_121.

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Rich, Peter R., and A. John Moody. "Cytochrome c oxidase." In Bioenergetics, 418–56. Basel: Birkhäuser Basel, 1997. http://dx.doi.org/10.1007/978-3-0348-8994-0_10.

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Hakvoort, T. B. M., G. J. C. Ruyter, K. M. C. Sinjorgo, and A. O. Muijsers. "Isoenzymes of Human Cytochrome c Oxidase." In Cytochrome Systems, 343–44. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_47.

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Bisson, Roberto. "Cytochrome c Oxidase: Structure." In Bioelectrochemistry III, 125–75. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4757-9459-5_7.

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Peters, Nils, Martin Dichgans, Sankar Surendran, Josep M. Argilés, Francisco J. López-Soriano, Sílvia Busquets, Klaus Dittmann, et al. "Cytochrome-C-Oxidase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 489–91. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_447.

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Capitanio, N., E. De Nitto, and S. Papa. "Protonmotive Activity of Mitochondrial Cytochrome c Oxidase." In Cytochrome Systems, 787–88. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_107.

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Müller, Michele, Nestor Labonia, Beatrice Schläpfer, and Angelo Azzi. "Cytochrome C Oxidase: Past, Present and Future." In Cytochrome Systems, 239–46. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_32.

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Alleyne, T., and M. T. Wilson. "Redox-Linked Conformational Changes in Cytochrome C Oxidase." In Cytochrome Systems, 713–20. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_100.

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Alben, James O. "Polarization in Heme Proteins and Cytochrome C Oxidase." In Cytochrome Systems, 361–69. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_50.

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Malmström, Bo G. "The Mechanism of Electron Gating in Cytochrome c Oxidase." In Cytochrome Systems, 733–41. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_102.

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Conference papers on the topic "Cytochrome C oxidase"

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Hsieh, Huai-Ching, Wen-Wei Tseng, and An-Chi Wei. "Mathematical model of photobiomodulation on cytochrome c oxidase." In 2022 IEEE 22nd International Conference on Bioinformatics and Bioengineering (BIBE). IEEE, 2022. http://dx.doi.org/10.1109/bibe55377.2022.00048.

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Rousseau, Denis L., Yuan-chin Ching, Sanghwa Han, Massimo Sassaroli, and Satish Singh. "Cytochrome C Oxidase: The Influence Of The "Open-Closed" Transition On Cytochrome A 3." In OE/LASE '89, edited by Fran Adar, James E. Griffiths, and Jeremy M. Lerner. SPIE, 1989. http://dx.doi.org/10.1117/12.951595.

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de Roever, Isabel, Gemma Bale, Robert J. Cooper, and Ilias Tachtsidis. "Cytochrome-C-Oxidase Exhibits Higher Brain-Specificity than Haemoglobin in Functional Activation." In Optics and the Brain. Washington, D.C.: OSA, 2016. http://dx.doi.org/10.1364/brain.2016.bth4d.4.

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OLEYNIKOV, I. P., N. V. AZARKINA, T. V. VYGODINA, and A. A. KONSTANTINOV. "THE DIRECT INTERACTION OF HORMONES WITH CYTOCHROME C OXIDASE FROM BOVINE HEART." In HOMO SAPIENS LIBERATUS. TORUS PRESS, 2020. http://dx.doi.org/10.30826/homosapiens-2020-29.

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Vasko, Vasyl V., Athanasios Bikas, Aneeta Patel, John Costello, Rok Tkavc, Kenneth D. Burman, and Kirk Jensen. "Abstract 1001: Expression of cytochrome C oxidase 4 (COX4) in thyroid cancer cells." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-1001.

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Börsch, Michael. "Targeting cytochrome C oxidase in mitochondria with Pt(II)-porphyrins for photodynamic therapy." In BiOS, edited by David H. Kessel. SPIE, 2010. http://dx.doi.org/10.1117/12.841284.

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Schonfeld, Justin, and Dan Ashlock. "Classifying Cytochrome c Oxidase subunit 1 by translation initiation mechanism using side effect machines." In 2010 IEEE Symposium on Computational Intelligence in Bioinformatics and Computational Biology (CIBCB). IEEE, 2010. http://dx.doi.org/10.1109/cibcb.2010.5510703.

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Dyer, R. B., Kristen A. Peterson, Page O. Stoutland, Oloef Einarsdottir, and William H. Woodruff. "Time-resolved infrared studies of the dynamics of ligand binding to cytochrome c oxidase." In Optics, Electro-Optics, and Laser Applications in Science and Engineering, edited by Robert R. Birge and Laurence A. Nafie. SPIE, 1991. http://dx.doi.org/10.1117/12.44223.

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Takano, Yu, Haruki Nakamura, Theodore E. Simos, George Maroulis, George Psihoyios, and Ch Tsitouras. "A Theoretical Approach to a Novel Pathway of Proton Translocation of Cytochrome c Oxidase." In SELECTED PAPERS FROM ICNAAM-2007 AND ICCMSE-2007: Special Presentations at the International Conference on Numerical Analysis and Applied Mathematics 2007 (ICNAAM-2007), held in Corfu, Greece, 16–20 September 2007 and of the International Conference on Computational Methods in Sciences and Engineering 2007 (ICCMSE-2007), held in Corfu, Greece, 25–30 September 2007. AIP, 2008. http://dx.doi.org/10.1063/1.2997316.

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Ramzan, R., P. Cybulski, V. Ruppert, P. Weber, M. Irqsusi, N. Mirow, A. Rastan, and S. Vogt. "Does MRNA Upregulation of Cytochrome C Oxidase Subunit 4 Isoform 2 Sustain Atrial Fibrillation?" In 50th Annual Meeting of the German Society for Thoracic and Cardiovascular Surgery (DGTHG). Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1725838.

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Reports on the topic "Cytochrome C oxidase"

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Minchev, Danail, Nikolay Popov, Veselin Petrov, Ivan Minkov, and Tihomir Vachev. Identification of a Novel Mitochondrial Mutation in the Cytochrome C Oxidase III Gene in Children with Autistic Sprectrum Disorders Using Next Generation RNA-Sequencing. "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, February 2021. http://dx.doi.org/10.7546/crabs.2021.02.09.

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Palmer, R. A. [An experiment in time-resolved step-scan FT-IR for use in dynamic photophysical studies of cytochrome-C oxidase and other heme proteins]. Final report. Office of Scientific and Technical Information (OSTI), July 1993. http://dx.doi.org/10.2172/10183410.

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Ohad, Itzhak, and Himadri Pakrasi. Role of Cytochrome B559 in Photoinhibition. United States Department of Agriculture, December 1995. http://dx.doi.org/10.32747/1995.7613031.bard.

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The aim of this research project was to obtain information on the role of the cytochrome b559 in the function of Photosystem-II (PSII) with special emphasis on the light induced photo inactivation of PSII and turnover of the photochemical reaction center II protein subunit RCII-D1. The major goals of this project were: 1) Isolation and sequencing of the Chlamydomonas chloroplast psbE and psbF genes encoding the cytochrome b559 a and b subunits respectively; 2) Generation of site directed mutants and testing the effect of such mutation on the function of PSII under various light conditions; 3) To obtain further information on the mechanism of the light induced degradation and replacement of the PSII core proteins. This information shall serve as a basis for the understanding of the role of the cytochrome b559 in the process of photoinhibition and recovery of photosynthetic activity as well as during low light induced turnover of the D1 protein. Unlike in other organisms in which the psbE and psbF genes encoding the a and b subunits of cytochrome b559, are part of an operon which also includes the psbL and psbJ genes, in Chlamydomonas these genes are transcribed from different regions of the chloroplast chromosome. The charge distribution of the derived amino-acid sequences of psbE and psbF gene products differs from that of the corresponding genes in other organisms as far as the rule of "positive charge in" is concerned relative to the process of the polypeptide insertion in the thylakoid membrane. However, the sum of the charges of both subunits corresponds to the above rule possibly indicating co-insertion of both subunits in the process of cytochrome b559 assembly. A plasmid designed for the introduction of site-specific mutations into the psbF gene of C. reinhardtii. was constructed. The vector consists of a DNA fragment from the chromosome of C. reinhardtii which spans the region of the psbF gene, upstream of which the spectinomycin-resistance-conferring aadA cassette was inserted. This vector was successfully used to transform wild type C. reinhardtii cells. The spectinomycin resistant strain thus obtained can grow autotrophically and does not show significant changes as compared to the wild-type strain in PSII activity. The following mutations have been introduced in the psbF gene: H23M; H23Y; W19L and W19. The replacement of H23 involved in the heme binding to M and Y was meant to permit heme binding but eventually alter some or all of the electron transport properties of the mutated cytochrome. Tryptophane W19, a strictly conserved residue, is proximal to the heme and may interact with the tetrapyrole ring. Therefore its replacement may effect the heme properties. A change to tyrosine may have a lesser affect on the potential or electron transfer rate while a replacement of W19 by leucine is meant to introduce a more prominent disturbance in these parameters. Two of the mutants, FW19L and FH23M have segregated already and are homoplasmic. The rest are still grown under selection conditions until complete segregation will be obtained. All mutants contain assembled and functional PSII exhibiting an increased sensitivity of PSII to the light. Work is still in progress for the detailed characterization of the mutants PSII properties. A tobacco mutant, S6, obtained by Maliga and coworkers harboring the F26S mutation in the b subunit was made available to us and was characterized. Measurements of PSII charge separation and recombination, polypeptide content and electron flow indicates that this mutation indeed results in light sensitivity. Presently further work is in progress in the detailed characterization of the properties of all the above mutants. Information was obtained demonstrating that photoinactivation of PSII in vivo initiates a series of progressive changes in the properties of RCII which result in an irreversible modification of the RCII-D1 protein leading to its degradation and replacement. The cleavage process of the modified RCII-D1 protein is regulated by the occupancy of the QB site of RCII by plastoquinone. Newly synthesized D1 protein is not accumulated in a stable form unless integrated in reassembled RCII. Thus the degradation of the irreversibly modified RCII-D1 protein is essential for the recovery process. The light induced degradation of the RCII-D1 protein is rapid in mutants lacking the pD1 processing protease such as in the LF-1 mutant of the unicellular alga Scenedesmus obliquus. In this case the Mn binding site of PSII is abolished, the water oxidation process is inhibited and harmful cation radicals are formed following light induced electron flow in PSII. In such mutants photo-inactivation of PSII is rapid, it is not protected by ligands binding at the QB site and the degradation of the inactivated RCII-D1 occurs rapidly also in the dark. Furthermore the degraded D1 protein can be replaced in the dark in absence of light driven redox controlled reactions. The replacement of the RCII-D1 protein involves the de novo synthesis of the precursor protein, pD1, and its processing at the C-terminus end by an unknown processing protease. In the frame of this work, a gene previously isolated and sequenced by Dr. Pakrasi's group has been identified as encoding the RCII-pD1 C-terminus processing protease in the cyanobacterium Synechocystis sp. PCC 6803. The deduced sequence of the ctpA protein shows significant similarity to the bovine, human and insect interphotoreceptor retinoid-binding proteins. Results obtained using C. reinhardtii cells exposes to low light or series of single turnover light flashes have been also obtained indicating that the process of RCII-D1 protein turnover under non-photoinactivating conditions (low light) may be related to charge recombination in RCII due to back electron flow from the semiquinone QB- to the oxidised S2,3 states of the Mn cluster involved in the water oxidation process.
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